2LOX: NMR structure of the complex between the PH domain of the Tfb1 subunit from TFIIH and Rad2

The general transcription factor IIH (TFIIH) plays crucial roles in transcription as part of the pre-initiation complex (PIC) and in DNA repair as part of the nucleotide excision repair (NER) machinery. During NER, TFIIH recruits the 3'-endonuclease Rad2 to damaged DNA. In this manuscript, we functionally and structurally characterized the interaction between the Tfb1 subunit of TFIIH and Rad2. We show that deletion of either the PH domain of Tfb1 (Tfb1PH) or several segments of the Rad2 spacer region yield yeast with enhanced sensitivity to UV irradiation. Isothermal titration calorimetry studies demonstrate that two acidic segments of the Rad2 spacer bind to Tfb1PH with nanomolar affinity. Structure determination of a Rad2-Tfb1PH complex indicates that Rad2 binds to TFIIH using a similar motif as TFIIEalpha uses to bind TFIIH in the PIC. Together, these results provide a mechanistic bridge between the role of TFIIH in transcription and DNA repair.
PDB ID: 2LOXDownload
MMDB ID: 97197
PDB Deposition Date: 2012/1/27
Updated in MMDB: 2012/07
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Biological Unit for 2LOX: dimeric; determined by author
Molecular Components in 2LOX
Label Count Molecule
Proteins (2 molecules)
RNA Polymerase II Transcription Factor B Subunit 1(Gene symbol: TFB1)
Molecule annotation
DNA Repair Protein Rad2(Gene symbol: RAD2)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB